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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human WDR46 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 39.58 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Lys187-Glu523 |
Aliases /Synonyms | WDR46, C6orf11, BING4, WD repeat-containing protein BING4, WD repeat-containing protein 46 |
Reference | ARO-P12083 |
Note | For research use only. |
Recombinant proteins have become essential tools in the field of biotechnology and medicine. These proteins are produced through genetic engineering techniques, allowing for the production of large quantities of pure protein with specific characteristics. One such recombinant protein is the Recombinant Human WDR46 Protein, which has gained attention for its unique structure, activity, and potential applications.
The WDR46 protein, also known as WD repeat-containing protein 46, is a highly conserved protein found in various species, including humans. The recombinant form of this protein is produced by inserting the gene encoding for WDR46 into a suitable expression vector, such as a bacterial or mammalian cell line. This allows for the production of a large quantity of pure protein.
The recombinant human WDR46 protein consists of 416 amino acids and has a molecular weight of approximately 47 kDa. It contains seven WD repeats, which are structural motifs commonly found in eukaryotic proteins. These repeats are responsible for the protein’s ability to interact with other proteins and form complexes.
Additionally, the recombinant human WDR46 protein has been shown to have a flexible structure, allowing it to adopt different conformations depending on its binding partners. This flexibility is crucial for the protein’s diverse functions and activities.
The main function of the WDR46 protein is to act as a co-chaperone for the molecular chaperone Hsp90. This means that it helps in the proper folding and stabilization of client proteins that are essential for various cellular processes, such as cell cycle regulation, signal transduction, and protein degradation.
In addition to its role as a co-chaperone, the recombinant human WDR46 protein has also been shown to interact with other proteins involved in DNA repair and transcriptional regulation. This suggests that it may have a broader role in maintaining cellular homeostasis and integrity.
Furthermore, studies have shown that the recombinant human WDR46 protein is essential for cell survival and proliferation, and its dysfunction has been linked to various diseases, including cancer and neurodegenerative disorders.
The unique structure and activity of the recombinant human WDR46 protein make it a valuable tool in various research fields. One of its main applications is in studying the mechanisms of protein folding and chaperone-mediated protein quality control. Its ability to form complexes with other proteins also makes it useful for studying protein-protein interactions.
Moreover, the recombinant human WDR46 protein has potential therapeutic applications. As it is involved in various cellular processes, it may serve as a target for drug development. Additionally, its role in DNA repair and transcriptional regulation makes it a potential biomarker for disease diagnosis and prognosis.
In summary, the recombinant human WDR46 protein is a crucial protein with a unique structure and activity. Its role as a co-chaperone and its involvement in various cellular processes make it a valuable tool in research and a potential target for therapeutic interventions. Further studies on this protein may lead to a better understanding of its functions and potential applications in the future.
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